Q8TEX9 · IPO4_HUMAN

  • Protein
    Importin-4
  • Gene
    IPO4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Nuclear transport receptor that mediates nuclear import of proteins, such as histones, RPS3A, TNP2 and VDR (PubMed:11823430, PubMed:16207705, PubMed:17682055, PubMed:21454524).
Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11823430, PubMed:16207705).
Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11823430, PubMed:16207705).
At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran (PubMed:11823430).
The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11823430).
Mediates the nuclear import of the histone H3-H4 dimer when in complex with ASF1 (ASF1A or ASF1B) (PubMed:21454524, PubMed:29408485).
Mediates the ligand-independent nuclear import of vitamin D receptor (VDR) (PubMed:16207705).
In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS (PubMed:12610148).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentcytoplasm
Cellular Componentmembrane
Cellular Componentnucleus
Cellular Componentprotein-containing complex
Molecular Functionnuclear import signal receptor activity
Molecular Functionnuclear localization sequence binding
Molecular Functionsmall GTPase binding
Biological Processprotein import into nucleus
Biological Processprotein localization to nucleus

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Importin-4
  • Short names
    Imp4
  • Alternative names
    • Importin-4b
      (Imp4b
      )
    • Ran-binding protein 4 (RanBP4)

Gene names

    • Name
      IPO4
    • Synonyms
      IMP4B, RANBP4

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q8TEX9
  • Secondary accessions
    • B2RN95
    • Q2NL96
    • Q86TZ9
    • Q8NCG8
    • Q96SJ3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_030758513in dbSNP:rs7146310
Natural variantVAR_030759580in dbSNP:rs11550452

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2,134 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue1UniProtN-acetylmethionine
ChainPRO_00001207481-1081UniProtImportin-4
Modified residue (large scale data)972PRIDEPhosphoserine
Modified residue (large scale data)1081PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Found in a cytosolic complex with ASF1 (ASF1A or ASF1B) and histones H3 and H4.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, repeat.

TypeIDPosition(s)Description
Domain24-90Importin N-terminal
Repeat348-385HEAT 1
Repeat390-427HEAT 2
Repeat431-471HEAT 3
Repeat475-513HEAT 4
Repeat895-932HEAT 5
Repeat936-974HEAT 6

Sequence similarities

Belongs to the importin beta family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8TEX9-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,081
  • Mass (Da)
    118,715
  • Last updated
    2007-02-20 v2
  • Checksum
    36D11AF0D6DA8B1E
MESAGLEQLLRELLLPDTERIRRATEQLQIVLRAPAALPALCDLLASAADPQIRQFAAVLTRRRLNTRWRRLAAEQRESLKSLILTALQRETEHCVSLSLAQLSATIFRKEGLEAWPQLLQLLQHSTHSPHSPEREMGLLLLSVVVTSRPEAFQPHHRELLRLLNETLGEVGSPGLLFYSLRTLTTMAPYLSTEDVPLARMLVPKLIMAMQTLIPIDEAKACEALEALDELLESEVPVITPYLSEVLTFCLEVARNVALGNAIRIRILCCLTFLVKVKSKALLKNRLLPPLLHTLFPIVAAEPPPGQLDPEDQDSEEEELEIELMGETPKHFAVQVVDMLALHLPPEKLCPQLMPMLEEALRSESPYQRKAGLLVLAVLSDGAGDHIRQRLLPPLLQIVCKGLEDPSQVVRNAALFALGQFSENLQPHISSYSREVMPLLLAYLKSVPLGHTHHLAKACYALENFVENLGPKVQPYLPELMECMLQLLRNPSSPRAKELAVSALGAIATAAQASLLPYFPAIMEHLREFLLTGREDLQPVQIQSLETLGVLARAVGEPMRPLAEECCQLGLGLCDQVDDPDLRRCTYSLFAALSGLMGEGLAPHLEQITTLMLLSLRSTEGIVPQYDGSSSFLLFDDESDGEEEEELMDEDVEEEDDSEISGYSVENAFFDEKEDTCAAVGEISVNTSVAFLPYMESVFEEVFKLLECPHLNVRKAAHEALGQFCCALHKACQSCPSEPNTAALQAALARVVPSYMQAVNRERERQVVMAVLEALTGVLRSCGTLTLKPPGRLAELCGVLKAVLQRKTACQDTDEEEEEEDDDQAEYDAMLLEHAGEAIPALAAAAGGDSFAPFFAGFLPLLVCKTKQGCTVAEKSFAVGTLAETIQGLGAASAQFVSRLLPVLLSTAQEADPEVRSNAIFGMGVLAEHGGHPAQEHFPKLLGLLFPLLARERHDRVRDNICGALARLLMASPTRKPEPQVLAALLHALPLKEDLEEWVTIGRLFSFLYQSSPDQVIDVAPELLRICSLILADNKIPPDTKAALLLLLTFLAKQHTDSFQAALGSLPVDKAQELQAVLGLS

Q8TEX9-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YMR4H0YMR4_HUMANIPO4547
H0YN07H0YN07_HUMANIPO4312
H0YN14H0YN14_HUMANIPO4911
H0YLV0H0YLV0_HUMANIPO498
H0YKG5H0YKG5_HUMANIPO4154
H0YL92H0YL92_HUMANIPO4101
H0YK93H0YK93_HUMANIPO448

Sequence caution

The sequence BAB15616.1 differs from that shown. Reason: Frameshift
The sequence BAB55421.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAC11174.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAD62595.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict865in Ref. 7; BAB15616
Sequence conflict943in Ref. 7; BAB55421
Alternative sequenceVSP_0093391038in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF411122
EMBL· GenBank· DDBJ
AAL78660.1
EMBL· GenBank· DDBJ
mRNA
BX248267
EMBL· GenBank· DDBJ
CAD62595.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AL136295
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471078
EMBL· GenBank· DDBJ
EAW66078.1
EMBL· GenBank· DDBJ
Genomic DNA
BC003690
EMBL· GenBank· DDBJ
AAH03690.2
EMBL· GenBank· DDBJ
mRNA
BC110804
EMBL· GenBank· DDBJ
AAI10805.1
EMBL· GenBank· DDBJ
mRNA
BC136759
EMBL· GenBank· DDBJ
AAI36760.1
EMBL· GenBank· DDBJ
mRNA
AK026991
EMBL· GenBank· DDBJ
BAB15616.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK027871
EMBL· GenBank· DDBJ
BAB55421.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK074743
EMBL· GenBank· DDBJ
BAC11174.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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